Difference between revisions of "AraN"
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** [[AraN]](2)-([[AraP]]-[[AraQ]])-[[MsmX]] {{PubMed|20693325}} | ** [[AraN]](2)-([[AraP]]-[[AraQ]])-[[MsmX]] {{PubMed|20693325}} | ||
− | * '''Localization:''' cell membrane (via [[AraP]]-[[AraQ]]) {{PubMed|10092453}} | + | * '''[[Localization]]:''' cell membrane (via [[AraP]]-[[AraQ]]) {{PubMed|10092453}} |
=== Database entries === | === Database entries === |
Revision as of 18:36, 16 July 2011
- Description: L-arabinose ABC transporter (sugar-binding protein)
Gene name | araN |
Synonyms | yseC |
Essential | no |
Product | L-arabinose ABC transporter (sugar-binding protein)) |
Function | uptake of arabinose |
Metabolic function and regulation of this protein in SubtiPathways: Sugar catabolism | |
MW, pI | 48 kDa, 8.555 |
Gene length, protein length | 1299 bp, 433 aa |
Immediate neighbours | araP, araM |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
Categories containing this gene/protein
ABC transporters, utilization of specific carbon sources, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU28750
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: bacterial solute-binding protein 1 family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization: cell membrane (via AraP-AraQ) PubMed
Database entries
- Structure:
- UniProt: P94528
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Additional publications: PubMed